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A6103

Sigma-Aldrich

Aprotinin

recombinant, expressed in Nicotiana (tobacco), ≥5 TIU/mg protein, powder, ≥98% (SDS-PAGE), suitable for inhibition assay

Synonyme(s) :

BPTI, Basic pancreatic trypsin inhibitor, Kallikrein-trypsin inactivator, Kunitz protease inhibitor

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About This Item

Numéro CE :
Code UNSPSC :
12352202
Nomenclature NACRES :
NA.77

product name

Aprotinin Nicotiana tobacco, >= 5TIU/mg protein, >= 98 % SDS-PAGE | 9087-70-1, recombinant, expressed in Nicotiana (tobacco), ≥5 TIU/mg protein, ≥98% (SDS-PAGE)

Produit recombinant

expressed in Nicotiana (tobacco)

Description

recombinant form of thenative bovine-sequence aprotinin purified from plant tissue (tobacco)

Gamme de produits

BioUltra

Pureté

≥98% (SDS-PAGE)

Forme

powder

Activité spécifique

≥5 TIU/mg protein

Poids mol.

~_6.5 kDa

Technique(s)

inhibition assay: suitable

Solubilité

0.85% sodium chloride: 5 mg/mL

Numéro d'accès UniProt

Température de stockage

2-8°C

Informations sur le gène

cow ... PTI(404172)

Définition de l'unité

One trypsin inhibitor unit (TIU) will decrease the activity of 2 trypsin units by 50% where one trypsin unit will hydrolyze 1.0 μmole of N-α-benzoyl-DL-arginine p-nitroanilide (BAPNA) per min at pH 7.8 at 25 °C.

Notes préparatoires

Contains no animal-derived components or impurities, and is manufactured by transient expression of the aprotinin message in RNA (+)-strand tobacco mosaic virus vectors propagated in non-transgenic Nicotiana plants. This is a recombinant form of the native, bovine-sequence aprotinin, which is traditionally isolated from bovine lung by methods involving fractional precipitation, gel filtration, and ion exchange chromatography. Unlike animal-derived aprotinin, this product is isolated and purified from plant tissue by proprietary methods.

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 1

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, type N95 (US)


Certificats d'analyse (COA)

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Jerzy Dorosz et al.
Scientific reports, 9(1), 4019-4019 (2019-03-13)
The full length human histone 3 lysine 4 demethylase KDM5B (PLU-1/Jarid1B) has been studied using Hydrogen/Deuterium exchange mass spectrometry, homology modelling, sequence analysis, small angle X-ray scattering and electron microscopy. This first structure on an intact multi-domain Jumonji histone demethylase
Allen M Vong et al.
Journal of translational medicine, 9, 101-101 (2011-07-05)
Non Obese Diabetic mice lacking B cells (NOD.Igμ(null) mice) do not develop diabetes despite their susceptible background. Upon reconstitution of B cells using a chimera approach, animals start developing diabetes at 20 weeks of age. We have used the spectratyping
Xi-Qin Ding et al.
PloS one, 4(10), e7410-e7410 (2009-10-14)
Subretinal delivery of polyethylene glycol-substituted lysine peptide (CK30PEG)-compacted DNA nanoparticles results in efficient gene expression in retinal cells. This work evaluates the ocular safety of compacted DNA nanoparticles. CK30PEG-compacted nanoparticles containing an EGFP expression plasmid were subretinally injected in adult
Radmila Hrdlicková et al.
Molecular and cellular biology, 29(3), 929-941 (2008-12-03)
Telomerase activity is downregulated in somatic cells but is upregulated during the activation of cells of the immune system. The mechanism of this reactivation is not well understood. In this study, we demonstrated that interferon regulatory factor 4 (IRF-4) and
Shankha Satpathy et al.
Nature communications, 11(1), 532-532 (2020-01-29)
Cancer proteogenomics promises new insights into cancer biology and treatment efficacy by integrating genomics, transcriptomics and protein profiling including modifications by mass spectrometry (MS). A critical limitation is sample input requirements that exceed many sources of clinically important material. Here

Articles

While aprotinin and bovine pancreatic trypsin inhibitor (BPTI) are the same protein sequence, the term aprotinin is typically used when describing the protein derived from bovine lung.

ReadyShield® phosphatase and protease inhibitor cocktail FAQ for sample protection in a variety of cell types and tissue extracts, including mammalian, plant, and microbial samples. Our ReadyShield® Protease Inhibitor Cocktail is a non-freezing solution that contains inhibitors with a broad specificity for serine, cysteine, acid proteases and aminopeptidases.

ReadyShield® phosphatase and protease inhibitor cocktail FAQ for sample protection in a variety of cell types and tissue extracts, including mammalian, plant, and microbial samples. Our ReadyShield® Protease Inhibitor Cocktail is a non-freezing solution that contains inhibitors with a broad specificity for serine, cysteine, acid proteases and aminopeptidases.

ReadyShield® phosphatase and protease inhibitor cocktail FAQ for sample protection in a variety of cell types and tissue extracts, including mammalian, plant, and microbial samples. Our ReadyShield® Protease Inhibitor Cocktail is a non-freezing solution that contains inhibitors with a broad specificity for serine, cysteine, acid proteases and aminopeptidases.

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Protocoles

Objective: To standardize a procedure for the enzymatic assay of Aprotinin.

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